EX1_ECOLI
ID EX1_ECOLI Reviewed; 475 AA.
AC P04995;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Exodeoxyribonuclease I;
DE Short=ExoI {ECO:0000303|PubMed:11101894};
DE Short=Exonuclease I {ECO:0000303|PubMed:11101894};
DE EC=3.1.11.1 {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
DE AltName: Full=DNA deoxyribophosphodiesterase;
DE Short=dRPase;
GN Name=sbcB; Synonyms=cpeA, xonA; OrderedLocusNames=b2011, JW1993;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12;
RX PubMed=3539937; DOI=10.1016/s0021-9258(19)75948-1;
RA Phillips G.J., Kushner S.R.;
RT "Determination of the nucleotide sequence for the exonuclease I structural
RT gene (sbcB) of Escherichia coli K12.";
RL J. Biol. Chem. 262:455-459(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION AS A DRPASE.
RX PubMed=1329027; DOI=10.1093/nar/20.18.4699;
RA Sandigursky M., Franklin W.A.;
RT "DNA deoxyribophosphodiesterase of Escherichia coli is associated with
RT exonuclease I.";
RL Nucleic Acids Res. 20:4699-4703(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP DOMAIN.
RC STRAIN=K12 / DH5-alpha {ECO:0000303|PubMed:11101894};
RX PubMed=11101894; DOI=10.1038/81978;
RA Breyer W.A., Matthews B.W.;
RT "Structure of Escherichia coli exonuclease I suggests how processivity is
RT achieved.";
RL Nat. Struct. Biol. 7:1125-1128(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH DTMP PRODUCT AND
RP MAGNESIUM, COFACTOR, AND DOMAIN.
RC STRAIN=K12 {ECO:0000303|PubMed:18219121};
RX PubMed=18219121; DOI=10.1107/s090744490706012x;
RA Busam R.D.;
RT "Structure of Escherichia coli exonuclease I in complex with thymidine 5'-
RT monophosphate.";
RL Acta Crystallogr. D 64:206-210(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH SSB
RP TAIL PEPTIDE AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH
RP SSB, DOMAIN, SITES, AND MUTAGENESIS OF ARG-148; GLU-150; TYR-207; LYS-227;
RP GLN-311; ARG-316; GLU-318; ASP-319; ARG-327; LEU-331; ARG-338; GLN-448 AND
RP GLN-452.
RX PubMed=18591666; DOI=10.1073/pnas.0800741105;
RA Lu D., Keck J.L.;
RT "Structural basis of Escherichia coli single-stranded DNA-binding protein
RT stimulation of exonuclease I.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH INHIBITORS AND
RP MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SSB, AND SITE.
RX PubMed=20018747; DOI=10.1073/pnas.0909191107;
RA Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.;
RT "Small-molecule tools for dissecting the roles of SSB/protein interactions
RT in genome maintenance.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH SINGLE-STRANDED
RP DNA SUBSTRATES AND ZINC.
RA Qiu R., Lou T., Wei J., Liu M., Gu S., Tang R., Ji C., Gong W.;
RT "The structures of Escherichia coli exonuclease I in complex with the
RT single strand DNA.";
RL Submitted (SEP-2012) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH SINGLE-STRANDED
RP DNA SUBSTRATES AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF HIS-181.
RC STRAIN=K12 {ECO:0000303|PubMed:23609540};
RX PubMed=23609540; DOI=10.1093/nar/gkt278;
RA Korada S.K., Johns T.D., Smith C.E., Jones N.D., McCabe K.A., Bell C.E.;
RT "Crystal structures of Escherichia coli exonuclease I in complex with
RT single-stranded DNA provide insights into the mechanism of processive
RT digestion.";
RL Nucleic Acids Res. 41:5887-5897(2013).
CC -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive
CC manner (PubMed:23609540). Also functions as a DNA
CC deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties
CC following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by
CC either an AP endonuclease or AP lyase (PubMed:1329027).
CC {ECO:0000269|PubMed:1329027, ECO:0000269|PubMed:23609540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1;
CC Evidence={ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747,
CC ECO:0000269|PubMed:23609540};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666,
CC ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:18591666};
CC -!- ACTIVITY REGULATION: Inhibited by 10 mM EDTA.
CC {ECO:0000269|PubMed:23609540}.
CC -!- SUBUNIT: Monomer (PubMed:23609540). Interacts with ssb (via C-
CC terminus); this interaction stimulates the exonuclease activity by
CC recruiting the enzyme to its substrate (PubMed:18591666,
CC PubMed:20018747). {ECO:0000269|PubMed:18591666,
CC ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}.
CC -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
CC terminal domain form a central positively charged groove which binds
CC the DNA. {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:23609540,
CC ECO:0000305|PubMed:11101894, ECO:0000305|PubMed:18219121}.
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DR EMBL; J02641; AAA19938.1; -; Unassigned_DNA.
DR EMBL; U00009; AAA16417.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75072.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15839.1; -; Genomic_DNA.
DR PIR; B64966; NCECX1.
DR RefSeq; NP_416515.1; NC_000913.3.
DR RefSeq; WP_000980589.1; NZ_LN832404.1.
DR PDB; 1FXX; X-ray; 2.40 A; A=1-475.
DR PDB; 2QXF; X-ray; 1.50 A; A=1-475.
DR PDB; 3C94; X-ray; 2.70 A; A=1-475.
DR PDB; 3C95; X-ray; 1.70 A; A=1-475.
DR PDB; 3HL8; X-ray; 1.55 A; A=1-475.
DR PDB; 3HP9; X-ray; 1.60 A; A=1-475.
DR PDB; 4HCB; X-ray; 2.00 A; A/B=1-475.
DR PDB; 4HCC; X-ray; 2.96 A; A/B=1-475.
DR PDB; 4JRP; X-ray; 1.95 A; A/B=1-475.
DR PDB; 4JRQ; X-ray; 3.00 A; A/B=1-475.
DR PDB; 4JS4; X-ray; 3.10 A; A/B=1-475.
DR PDB; 4JS5; X-ray; 3.50 A; A/B=1-475.
DR PDBsum; 1FXX; -.
DR PDBsum; 2QXF; -.
DR PDBsum; 3C94; -.
DR PDBsum; 3C95; -.
DR PDBsum; 3HL8; -.
DR PDBsum; 3HP9; -.
DR PDBsum; 4HCB; -.
DR PDBsum; 4HCC; -.
DR PDBsum; 4JRP; -.
DR PDBsum; 4JRQ; -.
DR PDBsum; 4JS4; -.
DR PDBsum; 4JS5; -.
DR AlphaFoldDB; P04995; -.
DR SMR; P04995; -.
DR BioGRID; 4260414; 102.
DR DIP; DIP-10827N; -.
DR IntAct; P04995; 7.
DR STRING; 511145.b2011; -.
DR jPOST; P04995; -.
DR PaxDb; P04995; -.
DR PRIDE; P04995; -.
DR EnsemblBacteria; AAC75072; AAC75072; b2011.
DR EnsemblBacteria; BAA15839; BAA15839; BAA15839.
DR GeneID; 946529; -.
DR KEGG; ecj:JW1993; -.
DR KEGG; eco:b2011; -.
DR EchoBASE; EB0919; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_6; -.
DR InParanoid; P04995; -.
DR OMA; RDRPAQF; -.
DR PhylomeDB; P04995; -.
DR BioCyc; EcoCyc:EG10926-MON; -.
DR BioCyc; MetaCyc:EG10926-MON; -.
DR BRENDA; 3.1.11.1; 2026.
DR EvolutionaryTrace; P04995; -.
DR PRO; PR:P04995; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
DR GO; GO:0008852; F:exodeoxyribonuclease I activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006308; P:DNA catabolic process; IDA:EcoCyc.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR023607; Exodeoxyribonuclease_I.
DR InterPro; IPR034748; EXOI_C.
DR InterPro; IPR034747; EXOI_SH3.
DR InterPro; IPR038649; EXOI_SH3_sf.
DR InterPro; IPR013620; Exonuc_1_C.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; PTHR11046; 1.
DR Pfam; PF08411; Exonuc_X-T_C; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51785; EXOI_C; 1.
DR PROSITE; PS51784; EXOI_SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Zinc.
FT CHAIN 1..475
FT /note="Exodeoxyribonuclease I"
FT /id="PRO_0000087110"
FT DOMAIN 13..192
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 202..355
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT DOMAIN 358..475
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11101894,
FT ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666,
FT ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18219121"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18219121"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18219121"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18219121"
FT SITE 18
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 66
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 113
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 124
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 128
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 142
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 148
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000269|PubMed:18591666"
FT SITE 164
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540,
FT ECO:0007744|PDB:4HCC"
FT SITE 181
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 207
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000269|PubMed:18591666"
FT SITE 214
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 257
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540,
FT ECO:0007744|PDB:4HCC"
FT SITE 284
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 304
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540,
FT ECO:0007744|PDB:4HCC"
FT SITE 311
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000269|PubMed:18591666"
FT SITE 338
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000305|PubMed:20018747"
FT SITE 368
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT SITE 371
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000269|PubMed:23609540"
FT MUTAGEN 148
FT /note="R->A: Strongly reduced ssb-binding. Reduced ssb-
FT dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 150
FT /note="E->A: About 2-fold increased ssb-binding. Weakly
FT increased ssb-independent and ssb-dependent nuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 181
FT /note="H->A: Residual nuclease activity."
FT /evidence="ECO:0000269|PubMed:23609540"
FT MUTAGEN 207
FT /note="Y->A: Strongly reduced ssb-binding. Reduced ssb-
FT dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 227
FT /note="K->A: 7-fold reduced ssb-binding. Reduced ssb-
FT dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 311
FT /note="Q->A: 2-fold reduced ssb-binding. Weakly reduced
FT ssb-dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 316
FT /note="R->A: Strongly reduced ssb-binding. Strongly reduced
FT ssb-dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 318
FT /note="E->A: About 2-fold increased ssb-binding. No effect
FT on ssb-dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 319
FT /note="D->A: 2-fold reduced ssb-binding. No effect on ssb-
FT dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 327
FT /note="R->A: No effect on ssb-binding and on ssb-dependent
FT nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 331
FT /note="L->A: No effect on ssb-binding and on ssb-dependent
FT nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 338
FT /note="R->A: 3-fold reduced ssb-binding. Reduced ssb-
FT dependent nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 448
FT /note="Q->A: No effect on ssb-binding and on ssb-dependent
FT nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT MUTAGEN 452
FT /note="Q->A: No effect on ssb-binding and on ssb-dependent
FT nuclease activity."
FT /evidence="ECO:0000269|PubMed:18591666"
FT CONFLICT 210..218
FT /note="Missing (in Ref. 1; AAA19938)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Q -> H (in Ref. 1; AAA19938)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="V -> E (in Ref. 1; AAA19938)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="V -> A (in Ref. 1; AAA19938)"
FT /evidence="ECO:0000305"
FT STRAND 10..21
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:2QXF"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:3HL8"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4HCB"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4JRQ"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4HCB"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 437..453
FT /evidence="ECO:0007829|PDB:2QXF"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:2QXF"
FT HELIX 458..473
FT /evidence="ECO:0007829|PDB:2QXF"
SQ SEQUENCE 475 AA; 54501 MW; A6A02AC17922C313 CRC64;
MMNDGKQQST FLFHDYETFG THPALDRPAQ FAAIRTDSEF NVIGEPEVFY CKPADDYLPQ
PGAVLITGIT PQEARAKGEN EAAFAARIHS LFTVPKTCIL GYNNVRFDDE VTRNIFYRNF
YDPYAWSWQH DNSRWDLLDV MRACYALRPE GINWPENDDG LPSFRLEHLT KANGIEHSNA
HDAMADVYAT IAMAKLVKTR QPRLFDYLFT HRNKHKLMAL IDVPQMKPLV HVSGMFGAWR
GNTSWVAPLA WHPENRNAVI MVDLAGDISP LLELDSDTLR ERLYTAKTDL GDNAAVPVKL
VHINKCPVLA QANTLRPEDA DRLGINRQHC LDNLKILREN PQVREKVVAI FAEAEPFTPS
DNVDAQLYNG FFSDADRAAM KIVLETEPRN LPALDITFVD KRIEKLLFNY RARNFPGTLD
YAEQQRWLEH RRQVFTPEFL QGYADELQML VQQYADDKEK VALLKALWQY AEEIV
